How to use Protein Binding Assay to Detect Properties of Proteins?
The Importance of Studying Protein-Protein Interactions
Aside from studying individual protein sequence and structures, expression profile, post-translational modifications and intracellular localization, you also need to investigate and analyze their interactions with other proteins. By knowing the functions of their binding partners, you will definitely get to know your proteins of interest a lot better. In fact, this is how a lot of previously unknown proteins have been discovered.
Studying protein-protein interactions is very important since it can:
Types of Protein-Protein Interactions and Their Biological Effects
Protein-protein interactions can be classified as either stable or transient. While stable interactions form stable complexes, transient interactions are more temporary in nature. However, these transient interactions are the ones that control most cellular processes.
Once a set of conditions are met, binding protein partners may interact with each other and bring about a wide range of cellular processes which may include cell cycling, protein modification, folding, transport and signaling.Proteins may bind with other proteins at specific binding domains through electrostatic interactions or salt bridges, hydrogen bonding, hydrophobic bonding and dipole-dipole interactions or van der Waals forces.
There are a number of biological effects that may result from the interaction of two or more proteins. Some interactions may alter the kinetic properties of an enzyme, create a new binding site or result in the production of an intended end product while some may serve a regulatory function in an upstream or downstream event. There are also some that may change the properties of a protein, inactivate it or totally destroy it.
Now that you understand why determining protein-protein interactions is extremely important, we will be discussing the many ways by which these interactions can be analyzed by using the appropriate protein binding assay in our next post.
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